THz time domain spectroscopy of biomolecular conformational modes.

Abstract:

:We discuss the use of terahertz time domain spectroscopy for studies of conformational flexibility and conformational change in biomolecules. Protein structural dynamics are vital to biological function with protein flexibility affecting enzymatic reaction rates and sensory transduction cycling times. Conformational mode dynamics occur on the picosecond timescale and with the collective vibrational modes associated with these large scale structural motions in the 1-100 cm(-1) range. We have performed THz time domain spectroscopy (TTDS) of several biomolecular systems to explore the sensitivity of TTDS to distinguish different molecular species, different mutations within a single species and different conformations of a given biomolecule. We compare the measured absorbances to normal mode calculations and find that the TTDS absorbance reflects the density of normal modes determined by molecular mechanics calculations, and is sensitive to both conformation and mutation. These early studies demonstrate some of the advantages and limitations of using TTDS for the study of biomolecules.

journal_name

Phys Med Biol

authors

Markelz A,Whitmire S,Hillebrecht J,Birge R

doi

10.1088/0031-9155/47/21/318

subject

Has Abstract

pub_date

2002-11-07 00:00:00

pages

3797-805

issue

21

eissn

0031-9155

issn

1361-6560

journal_volume

47

pub_type

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